@article{VanDerVenBartschGauteletal.2000,
  author    = {VanDerVen, Peter F. M. and Bartsch, J{\"o}rg and Gautel, Mathias and Jokusch, Harald and F{\"u}rst, Dieter Oswald},
  title     = {A functional knock-out of titin results in defective myofibril assembly},
  year      = {2000},
  language  = {en}
}
@article{SchroederVanDerVenWarloetal.2000,
  author    = {Schr{\"o}der, Rolf and VanDerVen, Peter F. M. and Warlo, Irene and Schumann, H. and F{\"u}rst, Dieter Oswald and Bl{\"u}mke, Ingmar and Goebel, Hans H. and Schmidt, M. C. and Hatzfeld, Mechthild},
  title     = {A member of the armadillo multigene family, is a constituent of sarcomeric I-bands in human skeletal muscle},
  year      = {2000},
  language  = {en}
}
@article{VorgerdvanderVenBruchertseiferetal.2005,
  author    = {Vorgerd, M. and vanderVen, Peter F. M. and Bruchertseifer, V. and Lowe, T. and Kley, R. A. and Schr{\"o}der, Rolf and Lochmuller, H. and Himmel, Mirko and Koehler, K. and F{\"u}rst, Dieter Oswald and Huebner, A.},
  title     = {A mutation in the dimerization domain of filamin C causes a novel type of autosomal dominant myofibrillar myopathy},
  issn      = {0002-9297},
  year      = {2005},
  abstract  = {Myofibrillar myopathy (MFM) is a human disease that is characterized by focal myofibrillar destruction and pathological cytoplasmic protein aggregations. In an extended German pedigree with a novel form of MFM characterized by clinical features of a limb-girdle myopathy and morphological features of MFM, we identified a cosegregating, heterozygous nonsense mutation (8130G -> A; W2710X) in the filamin c gene ( FLNC) on chromosome 7q32.1. The mutation is the first found in FLNC and is localized in the dimerization domain of filamin c. Functional studies showed that, in the truncated mutant protein, this domain has a disturbed secondary structure that leads to the inability to dimerize properly. As a consequence of this malfunction, the muscle fibers of our patients display massive cytoplasmic aggregates containing filamin c and several Z-disk-associated and sarcolemmal proteins},
  language  = {en}
}
@article{VanDerVenFuerst1997,
  author    = {VanDerVen, Peter F. M and F{\"u}rst, Dieter Oswald},
  title     = {Assembly of titin, myomesin and M-protein into the sarcomeric M-band in differentiating human skeletal muscle cells in vitro},
  year      = {1997},
  language  = {en}
}
@article{VanDerVenSpeelAlbrechtsetal.1999,
  author    = {VanDerVen, Peter F. M. and Speel, Ernst J. M. and Albrechts, Jozefa C. M. and Ramaekers, Frans C. S. and Hopman, Anton H. N. and F{\"u}rst, Dieter Oswald},
  title     = {Assignment of the human gene for endosarcomeric cytoskeletal M-protein (MYOM2) to 8p23.3},
  year      = {1999},
  language  = {en}
}
@article{SpeelVanDerVenAlbrechtsetal.1998,
  author    = {Speel, Ernst J. M. and VanDerVen, Peter F. M. and Albrechts, Jozefa C. M. and Ramaekers, Frans C. S. and F{\"u}rst, Dieter Oswald and Hopman, Anton H. N.},
  title     = {Assignment of the human gene for the sarcomeric M-band protein myomesin (MYOM1) to 18p11.31-p11.32},
  year      = {1998},
  language  = {en}
}
@article{VanDerVenSpeelAlbrechtsetal.1999,
  author    = {VanDerVen, Peter F. M. and Speel, Ernst J. M. and Albrechts, Jozefa C. M. and Ramaekers, Frans C. S. and Hopman, Anton H. N. and F{\"u}rst, Dieter Oswald},
  title     = {Chromosomal assignment of the human gene for endosarcomeric cytoskeletal M-protein (MYOM2) to 8p23.3},
  year      = {1999},
  language  = {en}
}
@article{SpeelVanDerVenAlbrechtsetal.1998,
  author    = {Speel, Ernst J. M. and VanDerVen, Peter F. M. and Albrechts, Jozefa C. M. and Hopman, Anton H. N. and F{\"u}rst, Dieter Oswald},
  title     = {Chromosomal assignment of the human myomesin gene},
  year      = {1998},
  language  = {en}
}
@article{GehmlichGeierOsterzieletal.2004,
  author    = {Gehmlich, Katja and Geier, C. and Osterziel, Karl Joseph and VanderVen, Peter F. M. and F{\"u}rst, Dieter Oswald},
  title     = {Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy},
  issn      = {0302-766X},
  year      = {2004},
  abstract  = {Previous work has shown that mutations in muscle LIM protein (MLP) can cause hypertrophic cardiomyopathy (HCM). In order to gain an insight into the molecular basis of the disease phenotype, we analysed the binding characteristics of wild-type MLP and of the (C58G) mutant MLP that causes hypertrophic cardiomyopathy. We show that MLP can form a ternary complex with two of its previously documented myofibrillar ligand proteins, N-RAP and alpha-actinin, which indicates the presence of distinct, non-overlapping binding sites. Our data also show that, in comparison to wild-type MLP, the capacity of the mutated MLP protein to bind both N-RAP and alpha-actinin is significantly decreased. In addition, this single point mutation prevents zinc coordination and proper folding of the second zinc-finger in the first LIM domain, which consequently renders the protein less stable and more susceptible to proteolysis. The molecular basis for HCM-causing mutations in the MLP gene might therefore be an alteration in the equilibrium of interactions of the ternary complex MLP-N-RAP-alpha-actinin. This assumption is supported by the previous observation that in the pathological situation accompanied by MLP down regulation, cardiomyocytes try to compensate for the decreased stability of MLP protein by increasing the expression of its ligand N-RAP, which might finally result in the development of myocyte disarray that is characteristic of this disease},
  language  = {en}
}
@article{VanDerVenFuerst1998,
  author    = {VanDerVen, Peter F. M and F{\"u}rst, Dieter Oswald},
  title     = {Expression of sarcomeric proteins and assembly of myofibrils in the putative myofibroblast cell line BHK-21/C13},
  year      = {1998},
  language  = {en}
}